The DOI matches its Crossref record; 48 of the 48 references it cites were found in a registry or an index.
Mycobacterial P1-Type ATPases Mediate Resistance to Zinc Poisoning in Human Macrophages
Open accessAbstract
Mycobacterium tuberculosis thrives within macrophages by residing in phagosomes and preventing them from maturing and fusing with lysosomes. A parallel transcriptional survey of intracellular mycobacteria and their host macrophages revealed signatures of heavy metal poisoning. In particular, mycobacterial genes encoding heavy metal efflux P-type ATPases CtpC, CtpG, and CtpV, and host cell metallothioneins and zinc exporter ZnT1, were induced during infection. Consistent with this pattern of gene modulation, we observed a burst of free zinc inside macrophages, and intraphagosomal zinc accumulation within a few hours postinfection. Zinc exposure led to rapid CtpC induction, and ctpC deficiency caused zinc retention within the mycobacterial cytoplasm, leading to impaired intracellular growth of the bacilli. Thus, the use of P(1)-type ATPases represents a M. tuberculosis strategy to neutralize the toxic effects of zinc in macrophages. We propose that heavy metal toxicity and its counteraction might represent yet another chapter in the host-microbe arms race.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The cited source says what the claim attributes to it.
In the citing paper
“Loss of Zn detoxification machinery in several bacterial pathogens, including Group A and B streptococci 166 , M. tuberculosis and S. pneumoniae , results in decreased intracellular survival 167-170 or in vivo survival in mouse models of infection 169 .”
From Nutritional immunity: the battle for nutrient metals at the host–pathogen interface (2022) · cites this paper as [167]
In the citing paper
“As with copper, M. tuberculosis express p-type ATPase to promote zinc efflux and to resist metal intoxication (239, 242).”
From Macrophage defense mechanisms against intracellular bacteria (2015) · cites this paper as [242]
In the citing paper
“Transcriptional profiling of M. tuberculosis in human macrophages identified signs of metal intoxication in bacteria and in the host, revealing a burst of free zinc in macrophages and intraphagosomal zinc accumulation (18).”
From Transition Metals and Virulence in Bacteria (2016) · cites this paper as [18]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence
Cole, S. T., Brosch, R., Parkhill, J., Garnier, T., Churcher, C., Harris, D., Gordon, S. V., Eiglmeier, K., Gas, S., Barry, C. E., et al. (1998) · Nature · doi:10.1038/31159 · Cited by 7,847
Exaptation—a missing term in the science of form
Gould, S. J., & Vrba, E. S. (1982) · Paleobiology · doi:10.1017/s0094837300004310 · Cited by 5,136
The Essential Toxin: Impact of Zinc on Human Health
Plum, L. M., Rink, L., & Haase, H. (2010) · International Journal of Environmental Research and Public Health · doi:10.3390/ijerph7041342 · Cited by 1,577
Natural resistance to infection with intracellular parasites: isolation of a candidate for Bcg
Vidal, S. M., Malo, D., Vogan, K., Skamene, E., & Gros, P. (1993) · Cell · doi:10.1016/0092-8674(93)90135-d · Cited by 1,104
Synthetic fluorescent sensors for studying the cell biology of metals
Domaille, D. W., Que, E. L., & Chang, C. J. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.69 · Cited by 1,085
Armstrong, J. A., & Hart, P. D. (1971) · The Journal of Experimental Medicine · doi:10.1084/jem.134.3.713 · Cited by 991
Regulation of metallothionein gene expression by oxidative stress and metal ions
Andrews, G. K. (2000) · Biochemical Pharmacology · doi:10.1016/s0006-2952(99)00301-9 · Cited by 834
Mammalian Zinc Transporters: Nutritional and Physiologic Regulation
Lichten, L. A., & Cousins, R. J. (2009) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-033009-083312 · Cited by 749
Nutritional immunity beyond iron: a role for manganese and zinc
Kehl-Fie, T. E., & Skaar, E. P. (2010) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2009.11.008 · Cited by 634
Zinc is a novel intracellular second messenger
Yamasaki, S., Sakata-Sogawa, K., Hasegawa, A., Suzuki, T., Kabu, K., Sato, E., Kurosaki, T., Yamashita, S., Tokunaga, M., Nishida, K., et al. (2007) · Journal of Cell Biology · doi:10.1083/jcb.200702081 · Cited by 592
Flagged first, then by citations
Cited by
Sorted by citations
Items 201–300 of 380
Cho, M., Hu, G., Caza, M., Horianopoulos, L. C., Kronstad, J. W., & Jung, W. H. (2018) · The Journal of Microbiology · doi:10.1007/s12275-018-7475-y · Cited by 17
Na-Phatthalung, P., Sun, S., Xie, E., Wang, J., Min, J., & Wang, F. (2024) · eLife · doi:10.7554/elife.89509 · Cited by 17
Gaballa, A., Sunil, S., Doll, E. V., Murphy, S. I., Bechtel, T. D., Guariglia-Oropeza, V., & Wiedmann, M. (2021) · PLoS ONE · doi:10.1371/journal.pone.0250989 · Cited by 15
Li, K., Gifford, A. H., Hampton, T. H., & O’Toole, G. A. (2019) · Journal of Bacteriology · doi:10.1128/jb.00618-19 · Cited by 18
Metal effect on intein splicing: A review
Panda, S., Nanda, A., Nasker, S. S., Sen, D., Mehra, A., & Nayak, S. (2021) · Biochimie · doi:10.1016/j.biochi.2021.03.006 · Cited by 17
Hanna, N., Burdet, F., Melotti, A., Bosmani, C., Kicka, S., Hilbi, H., Cosson, P., Pagni, M., & Soldati, T. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/590810 · Cited by 15
Serafini, A. (2021) · Microbiology · doi:10.1099/mic.0.001060 · Cited by 19
Nutritional immunity: targeting fungal zinc homeostasis
Alamir, O., Oladele, R. O., & Ibe, C. (2021) · Heliyon · doi:10.1016/j.heliyon.2021.e07805 · Cited by 17
An Improved Xer-cise Technology for the Generation of Multiple Unmarked Mutants in Mycobacteria
Boudehen, Y., Wallat, M., Rousseau, P., Neyrolles, O., & Gutierrez, C. (2020) · BioTechniques · doi:10.2144/btn-2019-0119 · Cited by 15
Self-citationChowdhury, D., Gardner, J. C., Satpati, A., Nookala, S., Mukundan, S., Porollo, A., Figueroa, J. A. L., & Vignesh, K. S. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.755961 · Cited by 14
ESX-3 secretion system in Mycobacterium: An overview
Granados-Tristán, A. L., Hernández-Luna, C. E., González-Escalante, L. A., Camacho-Moll, M. E., Silva-Ramírez, B., de León, M. B., & Peñuelas-Urquides, K. (2023) · Biochimie · doi:10.1016/j.biochi.2023.10.013 · Cited by 19
The role of transcriptional regulators in metal ion homeostasis of Mycobacterium tuberculosis
Wang, S., Ren, F., Wang, H., Li, X., Xing, J., Li, Z., & Song, N. (2024) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2024.1360880 · Cited by 16
Gonda, I., Sorrentino, S., Galazzo, L., Lichti, N. P., Arnold, F. M., Mehdipour, A. R., Bordignon, E., & Seeger, M. A. (2025) · Nature Communications · doi:10.1038/s41467-024-55136-7 · Cited by 17
The structure and activity of the glutathione reductase fromStreptococcus pneumoniae
Sikanyika, M., Aragão, D., McDevitt, C. A., & Maher, M. J. (2018) · Acta Crystallographica Section F Structural Biology Communications · doi:10.1107/s2053230x18016527 · Cited by 14
Portelinha, J., Heilemann, K., Jin, J., & Angeles-Boza, A. M. (2021) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2021.111391 · Cited by 14
Structure and ion-release mechanism of PIB-4-type ATPases
Grønberg, C., Hu, Q., Mahato, D. R., Longhin, E., Salustros, N., Duelli, A., Lyu, P., Bågenholm, V., Eriksson, J., Rao, K. U., et al. (2021) · eLife · doi:10.7554/elife.73124 · Cited by 16
Abrantes, M. C., Kok, J., & Lopes, M. D. F. S. (2014) · Microbiology · doi:10.1099/mic.0.080341-0 · Cited by 15
Quezada, L. A. L., Silve, S., Kelinske, M., Liba, A., Gonzalez, C. D., Kotev, M. I., Goullieux, L., Sans, S., Roubert, C., Lagrange, S., et al. (2019) · mBio · doi:10.1128/mbio.01405-19 · Cited by 15
Pulido, P. A., Novoa‐Aponte, L., Villamil, N., & Soto, C. Y. (2014) · Current Microbiology · doi:10.1007/s00284-014-0632-6 · Cited by 15
Francis, J. D., Guevara, M. A., Lu, J., Madhi, S. A., Kwatra, G., Aronoff, D. M., Manning, S. D., & Gaddy, J. A. (2022) · BMC Microbiology · doi:10.1186/s12866-021-02428-3 · Cited by 13
CFTR is required for zinc-mediated antibacterial defense in human macrophages
Gupta, K. D., Curson, J. E. B., Tarique, A. A., Kapétanovic, R., Schembri, M. A., Fantino, E., Sly, P. D., & Sweet, M. J. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2315190121 · Cited by 14
Midya, V., Agrawal, M., Lane, J. M., Gennings, C., Tarassishin, L., Torres-Olascoaga, L. A., Eggers, J., Gregory, J. K., Picker, M., Peter, I., et al. (2024) · Environment & Health · doi:10.1021/envhealth.4c00125 · Cited by 13
The influence of zinc levels on osteoarthritis: A comprehensive review
Tekeoğlu, İ., Şahin, M. Z., Kamanlı, A., & Nas, K. (2024) · Nutrition Research Reviews · doi:10.1017/s0954422424000234 · Cited by 13
RNA-based thermoregulation of a Campylobacter jejuni zinc resistance determinant
Barnawi, H., Masri, N., Hussain, N., Al-Lawati, B., Mayasari, E., Gulbicka, A., Jervis, A. J., Huang, M.-H., Cavet, J. S., & Linton, D. (2020) · PLoS Pathogens · doi:10.1371/journal.ppat.1009008 · Cited by 13
Kumari, M., Pal, R. K., Mishra, A., Tripathi, S., Biswal, B. K., Srivastava, K. K., & Arora, A. (2018) · Biochemical Journal · doi:10.1042/bcj20180356 · Cited by 13
Wang, A. S., Steers, N. J., Parab, A. R., Gachon, F., Sweet, M. J., & Mysorekar, I. U. (2022) · Mucosal Immunology · doi:10.1038/s41385-022-00558-z · Cited by 13
Zhai, P., Chai, Y., & Lü, L. (2022) · Microorganisms · doi:10.3390/microorganisms10122469 · Cited by 13
Iron, Copper, and Zinc Homeostasis in the Battle between Macrophage and Mycobacterium Tuberculosis
Yang, Z., Zhang, L., Wang, Y., Pi, J., Peng, D., Yao, Y., Xu, J., & Zhao, Y. (2024) · Current Medicinal Chemistry · doi:10.2174/0109298673283407231225140659 · Cited by 12
Structure and ion-release mechanism of PIB-4-type ATPases.
Grønberg, C., Hu, Q., Mahato, D. R., Longhin, E., Salustros, N., Duelli, A. S., Lyu, P., Bågenholm, V., Eriksson, J., Rao, K. U., et al. (2021) · Apollo (University of Cambridge) · doi:10.17863/cam.81891 · Cited by 12
Ribeiro, N. S., dos Santos, F. M., Garcia, A. W. A., Ferrareze, P. A. G., Fabres, L. F., Schrank, A., Kmetzsch, L., Rott, M. B., Vainstein, M. H., & Staats, C. C. (2017) · Frontiers in Microbiology · doi:10.3389/fmicb.2017.01626 · Cited by 12
Identification of zinc and Zur-regulated genes in Corynebacterium diphtheriae
Peng, E. D., & Schmitt, M. P. (2019) · PLoS ONE · doi:10.1371/journal.pone.0221711 · Cited by 11
Dhuldhaj, U. P., & Pandya, U. (2020) · Geomicrobiology Journal · doi:10.1080/01490451.2020.1817198 · Cited by 11
The TbD1 Locus Mediates a Hypoxia-Induced Copper Response in Mycobacterium bovis
Ma, R., Farrell, D., González, G., Browne, J. A., Nakajima, C., Suzuki, Y., & Gordon, S. V. (2022) · Frontiers in Microbiology · doi:10.3389/fmicb.2022.817952 · Cited by 11
Zhitnitsky, D., & Lewinson, O. (2013) · Molecular Microbiology · doi:10.1111/mmi.12495 · Cited by 11
Iron and Zinc Regulate Expression of a Putative ABC Metal Transporter in Corynebacterium diphtheriae
Peng, E. D., Oram, D. M., Battistel, M. D., Lyman, L. R., Freedberg, D. I., & Schmitt, M. P. (2018) · Journal of Bacteriology · doi:10.1128/jb.00051-18 · Cited by 11
Combating plant diseases through transition metal allocation
De, A., Hoang, C. V., Escudero, V., Armas, A. M., Echávarri‐Erasun, C., González‐Guerrero, M., & Jordá, L. (2024) · New Phytologist · doi:10.1111/nph.20366 · Cited by 12
Maya-Hoyos, M., Mata‐Espinosa, D., López-Torres, M. O., Tovar-Vázquez, B. E., Barrios‐Payán, J., León‐Contreras, J. C., Ocampo, M., Hernández‐Pando, R., & Soto, C. Y. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23116015 · Cited by 10
Chatterjee, D., Panda, A. P., Manasi, A. R. D., & Ghosh, A. S. (2024) · Microbiology · doi:10.1099/mic.0.001441 · Cited by 10
Li, T., Cao, H., Duan, C., Chen, S., & Xu, Z. (2024) · Applied and Environmental Microbiology · doi:10.1128/aem.02327-23 · Cited by 10
Self-harm to preferentially harm the pathogens within: non-specific stressors in innate immunity
LeGrand, E. K., & Day, J. (2016) · Proceedings of the Royal Society B Biological Sciences · doi:10.1098/rspb.2016.0266 · Cited by 9
dos Santos, F. M., Piffer, A. C., Schneider, R., Ribeiro, N. S., Garcia, A. W. A., Schrank, A., Kmetzsch, L., Vainstein, M. H., & Staats, C. C. (2017) · Future Microbiology · doi:10.2217/fmb-2016-0160 · Cited by 10
Murina, F., Lubrano, C., Cappelli, E., Campo, M., & Taraborrelli, S. (2022) · Health Care For Women International · doi:10.1080/07399332.2022.2061972 · Cited by 11
Transition metal cation inhibition of Mycobacterium tuberculosis esterase RV0045C
Bowles, I. E., Pool, E. H., Lancaster, B. S., Lawson, E. K., Savas, C. P., Kartje, Z. J., Severinac, L. E., Cho, D. H., Macbeth, M. R., Johnson, R. J., et al. (2021) · Protein Science · doi:10.1002/pro.4089 · Cited by 10
Visconti, S., Astolfi, M. L., Battistoni, A., & Ammendola, S. (2022) · Frontiers in Microbiology · doi:10.3389/fmicb.2022.975725 · Cited by 10
The Galvanizing of Mycobacterium tuberculosis: An Antimicrobial Mechanism
Russell, D. G. (2011) · Cell Host & Microbe · doi:10.1016/j.chom.2011.08.008 · Cited by 9
Callaghan, M. M., Klimowicz, A. K., Shockey, A. C., Kane, J., Pepperell, C. S., & Dillard, J. P. (2021) · Infection and Immunity · doi:10.1128/iai.00519-21 · Cited by 9
TRPV2, a novel player in the human ovary and human granulosa cells
Eubler, K., Caban, K. M., Dissen, G. A., Berg, U., Berg, D., Herrmann, C., Kreitmair, N., Tiefenbacher, A., Fröhlich, T., & Mayerhofer, A. (2023) · Molecular Human Reproduction · doi:10.1093/molehr/gaad029 · Cited by 8
Kwiatos, N., & Waldron, K. J. (2024) · Journal of Bacteriology · doi:10.1128/jb.00146-24 · Cited by 8
Mohsenpour, B., Ahmadi, A., Baneh, A. M., Hajibagheri, K., Ghaderi, E., Afrasiabian, S., & Azizi, S. (2019) · Medical Journal of the Islamic Republic of Iran · doi:10.47176/mjiri.33.33 · Cited by 8
Takács, T., Németh, M. T., Bohner, F., Vágvölgyi, C., Jankovics, F., Wilson, D., & Gácser, A. (2022) · Open Biology · doi:10.1098/rsob.220077 · Cited by 7
Martínez, D. P., Oyarzún, R., Quilapi, A. M., Coronado, J. L., Enríquez, R., Vargas‐Lagos, C., Oliver, C., Santibáñez, N., Godoy, M., Muñoz, J. L. P., et al. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1187209 · Cited by 7
Understanding the Development of Environmental Resistance Among Microbes: A Review
Srivastava, J., Chandra, H., Singh, N., & Kalra, S. J. S. (2016) · CLEAN - Soil Air Water · doi:10.1002/clen.201300975 · Cited by 8
Macrophage-Mediated Defensive Mechanisms Involving Zinc Homeostasis in Bacterial Infection
Na-Phatthalung, P., Min, J., & Wang, F. (2021) · Infectious Microbes & Diseases · doi:10.1097/im9.0000000000000058 · Cited by 8
Nguyen, H. N., Huynh, U., & Zastrow, M. L. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107840 · Cited by 7
López-R, M., Barrios‐Payán, J., Maya-Hoyos, M., Hernández‐Pando, R., Ocampo, M., Soto, C. Y., & Mata‐Espinosa, D. (2025) · Biomedicines · doi:10.3390/biomedicines13020439 · Cited by 6
Maure, A., Lawarée, E., Fiorentino, F., Pawlik, A., Gona, S., Giraud-Gatineau, A., Eldridge, M. J. G., Danckaert, A., Hardy, D., Frigui, W., et al. (2024) · PLoS Biology · doi:10.1371/journal.pbio.3002259 · Cited by 8
Self-citationInduction of Oral Lichen Planus–like Histopathology in Mice
Phuc, V. T.-D., Kang, M. G., Kim, H., Ko, Y. K., Acharya, S., Kim, E., Park, J., Chang, S. H., Kim, H. J., Yoon, H., et al. (2024) · Journal of Dental Research · doi:10.1177/00220345241304760 · Cited by 8
Mudarmah, K., Abeydeera, N., Chen, G., Jogadi, W., Krause, J. A., Budzik, J. M., & Huang, S. D. (2025) · Dalton Transactions · doi:10.1039/d4dt02895c · Cited by 8
Skariah, S., & Mordue, D. G. (2012) · PLoS ONE · doi:10.1371/journal.pone.0046621 · Cited by 7
Gouzy, A., Nigou, J., Gilleron, M., Neyrolles, O., Tailleux, L., & Gordon, S. V. (2012) · Research in Microbiology · doi:10.1016/j.resmic.2012.12.006 · Cited by 6
Self-citationSecli, V., Biagio, C. D., Martini, A., Michetti, E., Pacello, F., Ammendola, S., & Battistoni, A. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24020944 · Cited by 7
A brief history of metal recruitment in protozoan predation
Yu, Y., Li, Y., Ren, K., Hao, X., Fru, E. C., Rønn, R., Rivera, W. L., Becker, K., Feng, R., Yang, J., et al. (2023) · Trends in Microbiology · doi:10.1016/j.tim.2023.11.008 · Cited by 7
Metal regulation of Mycobacterium tuberculosis SufB intein splicing at the host–pathogen crossroad
Panda, S., Nanda, A., Nasker, S. S., Mehra, A., Ojha, D. K., Mohanty, P. S., & Nayak, S. (2023) · Clinical Science · doi:10.1042/cs20230307 · Cited by 5
Michetti, E., Mandava, T. A., Secli, V., Pacello, F., Battistoni, A., & Ammendola, S. (2025) · Microbiology · doi:10.1099/mic.0.001524 · Cited by 7
Janiszewski, L. N., Minson, M., Allen, M. A., Dowell, R. D., & Palmer, A. E. (2021) · Infection and Immunity · doi:10.1128/iai.00273-21 · Cited by 6
Antimicrobial Resistance inListeriaSpecies
Luque-Sastre, L., Arroyo, C., Fox, E. M., McMahon, B. J., Bai, L., Li, F., & Fanning, S. (2018) · ASM Press eBooks · doi:10.1128/9781555819804.ch11 · Cited by 6
Modulation of bacterial membrane proteins activity by clustering into plasma membrane nanodomains
Dupuy, P., Gutierrez, C., & Neyrolles, O. (2023) · Molecular Microbiology · doi:10.1111/mmi.15105 · Cited by 6
Self-citationNelson, S. J., Williams, J. T., Buglino, J. A., Nambi, S., Lojek, L. J., Glickman, M. S., Ioerger, T. R., & Sassetti, C. M. (2023) · mSphere · doi:10.1128/msphere.00389-22 · Cited by 6
Block, A. M., Nair, R. R., Meikle, V., Wiegert, P. C., White, D. W., Zhang, L., Niederweis, M., & Tischler, A. D. (2026) · mBio · doi:10.1128/mbio.03500-25 · Cited by 5
Mycobacterium tuberculosis adaptation to host environment
Banerjee, A., Sengupta, S., Nandanwar, N., Pandey, M., Tripathi, D., Pandey, S., Kumar, A., & Peddireddy, V. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-91806-0.00005-9 · Cited by 4
A bioinformatic analysis of zinc transporters in intestinal Lactobacillaceae
Huynh, U., Nguyen, H. N., Trinh, B. K., Elhaj, J., & Zastrow, M. L. (2023) · Metallomics · doi:10.1093/mtomcs/mfad044 · Cited by 5
Chalkophore-mediated respiratory oxidase flexibility controls M. tuberculosis virulencePreprint
Buglino, J. A., Ozakman, Y., Hatch, C. E., Benjamin, A., Tan, D. S., & Glickman, M. S. (2025) · eLife · doi:10.7554/elife.105794.3 · Cited by 9
Chung, H., & Bird, A. J. (2019) · Springer eBooks · doi:10.1007/978-981-15-0557-7_19 · Cited by 5
Grant, C. R., & Komeili, A. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.01.10.902569 · Cited by 5
Quantification of zinc intoxication of Candida glabrata after phagocytosis by primary macrophages
Penninger, P., Riedelberger, M., Tsymala, I., Arzani, H., Jenull, S., & Kuchler, K. (2021) · STAR Protocols · doi:10.1016/j.xpro.2021.100352 · Cited by 4
Ma, H., Wang, M., Yao, Y., Zhang, S., Wang, M., Zhu, D., Jia, R., Chen, S., Zhao, X., Yang, Q., et al. (2025) · Microbiology Spectrum · doi:10.1128/spectrum.03178-24 · Cited by 4
Vasanthrao, R., Nidhin, I. K., Taj, Z., & Chattopadhyay, I. (2025) · Frontiers in Microbiology · doi:10.3389/fmicb.2025.1649872 · Cited by 4
Bosc, L., Sécher, T., Ball, G., Pennec, D. L., Tribout, M., Ba, M., Bai, Y., Ouerdane, L., Arnoux, P., Denis, Y., et al. (2026) · Infection and Immunity · doi:10.1128/iai.00453-25 · Cited by 5
Mechanisms and Therapeutic Potential of Nutritional Immunity
Ugwu, C. E., Akinsulie, O. C., Ayandokun, T. F., Ajibade, F. A., Shahzad, S., Aliyu, V. A., Oladoye, M. J., Idris, I., Obasi, K. O., Edeh, J. K., et al. (2026) · Pathogens · doi:10.3390/pathogens15020176 · Cited by 4
Membrane-associated effluxosomes coordinate multi-metal resistance in Mycobacterium tuberculosis
Dupuy, P., Boudehen, Y., Faucher, M., Buglino, J. A., Fay, A., Cantaloube, S., Grimoire, Y., Marcoux, J., Levet, F., Bettarel, L., et al. (2026) · The EMBO Journal · doi:10.1038/s44318-026-00715-1 · Cited by 7
Self-citationSankova, M. V., Nikolenko, V. N., Oganesyan, M. V., Vinnik, Y. S., Владимировна, Г. Л., Redina, S., Rizaeva, N. A., Sankov, A. V., Bulygin, K. V., Vovkogon, A. D., et al. (2024) · Cytokine · doi:10.1016/j.cyto.2024.156761 · Cited by 5
LeGrand, E. K. (2025) · Frontiers in Nutrition · doi:10.3389/fnut.2025.1508767 · Cited by 4
IFIT2-induced transcriptomic changes in Mycobacterium tuberculosis infected macrophages
Manful, E.-E., Pietersen, R., & Baker, B. (2025) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2025.1536446 · Cited by 4
Zinc and the immune system: Insights into the role of zinc in autoimmune diseases
Gammoh, N. Z., & Rink, L. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-805378-2.00003-6 · Cited by 5
Metallobiology of Tuberculosis
Rodríguez, G. M., & Neyrolles, O. (2015) · ASM Press eBooks · doi:10.1128/9781555818845.ch19 · Cited by 4
Self-citationIs Oral Vaccination against Escherichia coli Influenced by Zinc Oxide?
Ramis, G., Murciano, F., Orengo, J., González-Guijarro, B., Cuellar-Flores, A., Serrano, D., Luna, A. M., Sánchez-Uribe, P., & Martínez-Alarcón, L. (2023) · Animals · doi:10.3390/ani13111754 · Cited by 4
A moonlighting function of Mycobacterium smegmatis Ku in zinc homeostasis?
Kushwaha, A. K., Deochand, D. K., & Grove, A. (2014) · Protein Science · doi:10.1002/pro.2612 · Cited by 4
Nanoscale chemical imaging of phagocytosis: A battle for metals between host and microbe
Ullah, N., Samber, B. D., Uwamahoro, N., Malderen, S. J. M. V., Sandblad, L., Bohic, S., Cloetens, P., Vincze, L., & Urban, C. F. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110485 · Cited by 3
Verrall, A. J., Houghton, L. A., Apriani, L., Atmaja, H. E., van Laarhoven, A., Ussher, J. E., Ruslami, R., SHARPLES, K. J., McAllister, S. M., van Crevel, R., et al. (2025) · Transactions of the Royal Society of Tropical Medicine and Hygiene · doi:10.1093/trstmh/trae140 · Cited by 3
Wong, T.-Y., Sharma, S., Mehdiratta, K., Bhosale, R. S., Nimmakayala, K., Wilharm, R. K., Chakraborty, A., Orimoloye, M. O., Liu, Q., Kamat, S. S., et al. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.5c13262 · Cited by 3
Effluxosomes and the evolution of metal resistance in Mycobacterium tuberculosis
Benastre, L., Dupuy, P., Gutierrez, C., Demange, P., & Neyrolles, O. (2026) · Infection and Immunity · doi:10.1128/iai.00307-26 · Cited by 3
Self-citationIdentification and characterization of zinc importers in Corynebacterium diphtheriae
Peng, E. D., Lyman, L. R., & Schmitt, M. P. (2024) · Journal of Bacteriology · doi:10.1128/jb.00124-24 · Cited by 3
Andrews, R. M., Bollar, G. E., Giattina, A. S., Dalecki, A. G., Wallace, J. R., Frantz, L., Eschliman, K., Covarrubias‐Zambrano, O., Keith, J. D., Duverger, A. E., et al. (2023) · Metallomics · doi:10.1093/mtomcs/mfad049 · Cited by 3
The influence of amoeba metal homeostasis on antifungal activity against Cryptococcus gattii
João, M. E. D., Tavanti, A. G., de Vargas, A. N., Kmetzsch, L., & Staats, C. C. (2024) · Genetics and Molecular Biology · doi:10.1590/1678-4685-gmb-2023-0320 · Cited by 3
Raynaud, S., Hallier, M., Dréano, S., Felden, B., Augagneur, Y., & Pabic, H. L. (2024) · RNA · doi:10.1261/rna.080122.124 · Cited by 3
Bohada, D. P., Bravo-Sanabria, K. D., Malpica, P. A. C., & Rodríguez, R. (2024) · Tropical Medicine and Infectious Disease · doi:10.3390/tropicalmed9090197 · Cited by 4
Role of Divalent Cations in Infections in Host–Pathogen Interaction
D’Elia, J. A., & Weinrauch, L. A. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25189775 · Cited by 3
The Important Role of Metal Ions for Survival of Francisella in Water within Amoeba Environment
Ožanić, M., Marečić, V., Knežević, M., Majstorović, A., Žurga, P., Ćurlin, M., Piškur, V., Lenac, D., Bulog, A., & Šantić, M. (2021) · BioMed Research International · doi:10.1155/2021/6673642 · Cited by 3
The Sculpting of theMycobacterium tuberculosisGenome by Host Cell–Derived Pressures
Russell, D. G., Lee, W., Tan, S., Sukumar, N., Podinovskaia, M., Fahey, R. J., & VanderVen, B. C. (2014) · Microbiology Spectrum · doi:10.1128/microbiolspec.mgm2-0016-2013 · Cited by 3
Metadata
- Authors
- Botella, H., Peyron, P., Levillain, F., Poincloux, R., Poquet, Y., Brandli, I., Wang, C., Tailleux, L., Tilleul, S., Charrière, G. M., Waddell, S. J., Foti, M., Lugo-Villarino, G., Gao, Q., Maridonneau-Parini, I., Butcher, P. D., Castagnoli, P. R., Gicquel, B., de Chastellier, C., & Neyrolles, O.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- Institut Pasteur (FR)
- Brighton and Sussex Medical School (GB)
- University of Milano-Bicocca (IT)
- Shanghai Medical College of Fudan University (CN)
- St George's, University of London (GB)
- Singapore Immunology Network (SG)
- Corresponding author
- Neyrolles, Olivier
- ORCID
- Venue
- Cell Host & Microbe
- Publisher
- Elsevier BV
- Published
- 2011-09
- Volume
- 10
- Issue
- 3
- Pages
- 248-259
- ISSN
- 1931-3128 (ISSN-L)
- PMC
- PMC3221041
- OpenAlex
- W2128702173
- Cited by
- 381
- References
- 48
- Citations by year
- 2026: 23 · 2025: 20 · 2024: 32 · 2023: 21 · 2022: 27 · 2021: 41 · 2020: 30 · 2019: 32 · 2018: 23 · 2017: 27 · 2016: 19 · 2015: 23 · 2014: 23 · 2013: 21 · 2012: 17
- FWCI
- 13.38
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Cell Host & Microbe (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Sussex Research Online (University of Sussex) (submittedVersion, cc-by)
- HAL (submittedVersion)
- HAL AMU (submittedVersion)
- BOA (University of Milano-Bicocca) (submittedVersion)
- Figshare (submittedVersion, cc-by)
- Funders
- Wellcome Trust (086547)
- Topics
- Health Sciences › Medicine › Infectious Diseases › Tuberculosis Research and Epidemiology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Health Sciences › Medicine › Epidemiology › Mycobacterium research and diagnosis
- Keywords
- Mycobacterium tuberculosis, zinc efflux, zinc toxicity, metallothionein, ZnT1, phagosome maturation, intracellular bacterial growth, macrophages
- MeSH terms
- Animals, Cells, Cultured, Female, Humans, Macrophages, Mice, Inbred BALB C, Mycobacterium tuberculosis, Tuberculosis, Zinc, Bacterial Proton-Translocating ATPases, Mice
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review